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cc-by-nc-sa (c) Spanish Society for Microbiology (SEM) and Viguera Editores SL, 2009
Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/33550

NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional housekeeping protein reported to be a target of several covalent modifications in many organisms. In a previous study we showed that enterohemorragic (EHEC) and enteropathogenic (EPEC) Escherichia coli strains secrete GAPDH and that this protein binds to human plasminogen and fibrinogen. Here we report that GAPDH of these pathogens is ADP-ribosylated either in the cytoplasm or in the extracellular medium. GAPDH catalyzes its own modification which involves Cys149 at the active site. ADP-ribosylation of extracellular GAPDH may play important role in the interaction with the host as it has been proposed in other pathogens.

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AGUILERA GIL, Maria Laura, et al. NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase. International Microbiology. 2009. Vol. 12, num. 3, pags. 187-192. ISSN 1139-6709. [consulted: 10 of August of 2026]. Available at: https://hdl.handle.net/2445/33550

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